Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 24, Pages 10039-10046Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja301297g
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Funding
- National Science Foundation [CHE-0094332, CHE-0840464]
- Robert A. Welch Foundation [A-1421, A-1658]
- Czech Science Foundation [203/08/0114]
- Academy of Sciences (Praemium Academie)
- International Max-Planck Research School
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0840464] Funding Source: National Science Foundation
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The specific binding sites of Hofmeister ions with an uncharged 600-residue elastin-like polypeptide, (VPGVG)(120), were elucidated using a combination of NMR and thermodynamic measurements along with molecular dynamics simulations. It was found that the large soft anions such as SCN- and I- interact with the polypeptide backbone via a hybrid binding site that consists of the amide nitrogen and the adjacent alpha-carbon. The hydrocarbon groups at these sites bear a slight positive charge, which enhances anion binding without disrupting specific hydrogen bonds to water molecules. The hydrophobic side chains do not contribute significantly to anion binding or the corresponding salting-in behavior of the biopolymer. Cl- binds far more weakly to the amide nitrogen/alpha-carbon binding site, while SO42- is repelled from both the backbone and hydrophobic side chains of the polypeptide. The Na+ counterions are also repelled from the polypeptide. The identification of these molecular-level binding sites provides new insights into the mechanism of peptide-anion interactions.
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